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Eukaryotic Cell, October 2003, p. 886-900, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.886-900.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Chitin Synthesis in Saccharomyces cerevisiae in Response to Supplementation of Growth Medium with Glucosamine and Cell Wall Stress

Dorota A. Bulik,1 Mariusz Olczak,1,{dagger} Hector A. Lucero,1 Barbara C. Osmond,1 Phillips W. Robbins,1 and Charles A. Specht2*

Department of Molecular and Cell Biology, School of Dental Medicine,1 Department of Medicine, School of Medicine, Boston University, Boston, Massachusetts 021182

Received 26 February 2003/ Accepted 10 July 2003

In Saccharomyces cerevisiae most chitin is synthesized by Chs3p, which deposits chitin in the lateral cell wall and in the bud-neck region during cell division. We have recently found that addition of glucosamine (GlcN) to the growth medium leads to a three- to fourfold increase in cell wall chitin levels. We compared this result to the increases in cellular chitin levels associated with cell wall stress and with treatment of yeast with mating pheromone. Since all three phenomena lead to increases in precursors of chitin, we hypothesized that chitin synthesis is at least in part directly regulated by the size of this pool. This hypothesis was strengthened by our finding that addition of GlcN to the growth medium causes a rapid increase in chitin synthesis without any pronounced change in the expression of more than 6,000 genes monitored with Affymetrix gene expression chips. In other studies we found that the specific activity of Chs3p is higher in the total membrane fractions from cells grown in GlcN and from mutants with weakened cell walls. Sucrose gradient analysis shows that Chs3p is present in an inactive form in what may be Golgi compartments but as an active enzyme in other intracellular membrane-bound vesicles, as well as in the plasma membrane. We conclude that Chs3p-dependent chitin synthesis in S. cerevisiae is regulated both by the levels of intermediates of the UDP-GlcNAc biosynthetic pathway and by an increase in the activity of the enzyme in the plasma membrane.

* Corresponding author. Mailing address: Department of Medicine, Boston University, 650 Albany St., EBRC-625, Boston, MA 02118. Phone: (617) 414-5284. Fax: (617) 414-5280. E-mail: cspecht{at}bu.edu.

{dagger} Present address: Institute of Biochemistry and Molecular Biology, Wroclaw University, 50-137 Wroclaw, Poland.

Eukaryotic Cell, October 2003, p. 886-900, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.886-900.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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